Solution structure of the bb' domains of human protein disulfide isomerase (Q27653624)

6

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David Y. Thomas

object named as

David Y Thomas

5

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author name string

Alexey Y Denisov

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Pekka Määttänen

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Christian Dabrowski

The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain

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language of work or name

English

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publication date

March 2009

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published in

FEBS Journal

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volume

276

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issue

5

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page(s)

1440-9

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cites work

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Protein disulfide isomerase: the structure of oxidative folding

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The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins

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Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy

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Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' domain

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Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution

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1H, 13C and 15N resonance assignments of the bb' domains of human protein disulfide isomerase.

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Crystal structure of the bb' domains of the protein disulfide isomerase ERp57

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PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.

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Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail

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Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase

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Effect of protein and peptide inhibitors on the activity of protein disulfide isomerase.

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